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| | ==High resolution x-ray structure of urate oxidase in complex with 8-azaxanthine== | | ==High resolution x-ray structure of urate oxidase in complex with 8-azaxanthine== |
| - | <StructureSection load='4n9v' size='340' side='right' caption='[[4n9v]], [[Resolution|resolution]] 1.10Å' scene=''> | + | <StructureSection load='4n9v' size='340' side='right'caption='[[4n9v]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n9v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N9V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N9V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9v OCA], [https://pdbe.org/4n9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n9v RCSB], [https://www.ebi.ac.uk/pdbsum/4n9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n9v ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iba|2iba]], [[4n3m|4n3m]], [[4n9m|4n9m]], [[4n9s|4n9s]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 ASPFL])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9v OCA], [http://pdbe.org/4n9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n9v RCSB], [http://www.ebi.ac.uk/pdbsum/4n9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n9v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL]] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. | + | [https://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Urate Oxidase|Urate Oxidase]] | + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspfl]] | + | [[Category: Aspergillus flavus]] |
| - | [[Category: Factor independent urate hydroxylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Blakeley, M P]] | + | [[Category: Blakeley MP]] |
| - | [[Category: Budayova-Spano, M]] | + | [[Category: Budayova-Spano M]] |
| - | [[Category: Oksanen, E]] | + | [[Category: Oksanen E]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Urate oxidase]]
| + | |
| - | [[Category: Uricase]]
| + | |
| Structural highlights
4n9v is a 1 chain structure with sequence from Aspergillus flavus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
URIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Publication Abstract from PubMed
Urate oxidase transforms uric acid to 5-hydroxyisourate without the help of cofactors, but the catalytic mechanism has remained enigmatic, as the protonation state of the substrate could not be reliably deduced. We have determined the neutron structure of urate oxidase, providing unique information on the proton positions. A neutron crystal structure inhibited by a chloride anion at 2.3 A resolution shows that the substrate is in fact 8-hydroxyxanthine, the enol tautomer of urate. We have also determined the neutron structure of the complex with the inhibitor 8-azaxanthine at 1.9 A resolution, showing the protonation states of the K10-T57-H256 catalytic triad. Together with X-ray data and quantum chemical calculations, these structures allow us to identify the site of the initial substrate protonation and elucidate why the enzyme is inhibited by a chloride anion.
The neutron structure of urate oxidase resolves a long-standing mechanistic conundrum and reveals unexpected changes in protonation.,Oksanen E, Blakeley MP, El-Hajji M, Ryde U, Budayova-Spano M PLoS One. 2014 Jan 23;9(1):e86651. doi: 10.1371/journal.pone.0086651. eCollection, 2014 Jan 23. PMID:24466188[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oksanen E, Blakeley MP, El-Hajji M, Ryde U, Budayova-Spano M. The neutron structure of urate oxidase resolves a long-standing mechanistic conundrum and reveals unexpected changes in protonation. PLoS One. 2014 Jan 23;9(1):e86651. doi: 10.1371/journal.pone.0086651. eCollection, 2014 Jan 23. PMID:24466188 doi:http://dx.doi.org/10.1371/journal.pone.0086651
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